Regulation of nuclear scaffold protease activity by calcium

Experimental Cell Research
K R MadsenG A Clawson

Abstract

Recent investigations have disclosed protease activity which is intimately associated with the nuclear scaffold. This protease activity shows a marked selectivity for lamins A/C, and from them may produce the 46-kDa NTPase thought to participate in nucleocytoplasmic RNA transport. Preliminary characterizations suggested that the protease activity might require Ca2+. In this report, we present evidence showing that nuclear scaffold protease activity is stringently regulated by Ca2+ within the physiologic range. Further, calmodulin antagonists such as calmidazolium and chlorpromazine produce marked inhibition of the protease activity, suggesting modulation by calmodulin or calmodulin-like factors.

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Citations

Sep 29, 2006·Journal of Cellular Biochemistry·Chetan DhamneGary A Clawson
Apr 1, 1991·Experimental Cell Research·A M Schwartz, G A Clawson
Jul 10, 1997·Experimental Cell Research·L Ren, G A Clawson
Oct 1, 1995·Hepatology : Official Journal of the American Association for the Study of Liver Diseases·G A ClawsonH C Isom
Mar 1, 1991·Hepatology : Official Journal of the American Association for the Study of Liver Diseases·G A ClawsonC L Hatem
Mar 28, 2006·Molecular Therapy : the Journal of the American Society of Gene Therapy·David A DrubinCraig Meyers
Oct 17, 2006·The Biochemical Journal·Richard Thorogate, Katalin Török

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